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UnknownThe Allosteric Regulation of the DNA-Binding Domain of p53 by the Intrinsically Disordered C-Terminal Domain.
Not available
S-EPMC12845269 | biostudies-literature
UnknownChromosome-Level Genome Assembly and Annotation of the Highly Heterozygous <i>Phallus echinovolvatus</i> Provide New Insights into Its Genetics.
Not available
S-EPMC11766896 | biostudies-literature
MetabolomicsAlterations in the gut microbiota and metabolic profiles coincide with intestinal damage in mice with a bloodborne Candida albicans infection
Candida albicans is an opportunistic fungus that can threaten life especially in patients with candidemia. The morbidity and mortality of candidemia originating from a central venous catheter (CVC) and illicit intravenous drug use (IVDU) are increasing. However, the mechanism underlying the bloodbor...
2021-04-13 | MTBLS1918 | MetaboLights
UnknownWeighted gene coexpression correlation network analysis reveals a potential molecular regulatory mechanism of anthocyanin accumulation under different storage temperatures in 'Friar' plum.
Not available
S-EPMC8647467 | biostudies-literature
UnknownOptical control of membrane tethering and interorganellar communication at nanoscales.
Not available
S-EPMC5606013 | biostudies-literature
ProteomicsQuantitative Proteome and Lysine Lactylome of Proteins in the Cortex of Sham and CCI Mouse
Quantitative proteome and lysine lactylome analyses were conducted on proteins extracted from the cortex of sham and controlled cortical impact (CCI) mice.
ORGANISM(S): Mus musculus (Mouse) 
2026-03-02 | PXD045802 | Pride
Mouse Lactylation Cortex 
ProteomicsIdentification of Tufm-interacting proteins by IP-MS/MS
Tufm-FLAG and its interacting proteins were enriched by immunoprecipitation using Anti-C-Flag Nanobody Agarose Beads. Then, Tufm-FLAG-interacting proteins were identified by mass spectrum.
ORGANISM(S): Homo sapiens (Human) 
2026-03-02 | PXD045404 | Pride
Mouse Mitochondria Ip-ms/ms Tufm 
UnknownVav2 is a novel APP-interacting protein that regulates APP protein level.
Not available
S-EPMC9325707 | biostudies-literature
ProteomicsComprehensive evaluation of cleavable bioorthogonal probes for site-specific O-GlcNAc proteomics
O-linked β-N-acetylglucosamine (O-GlcNAc) modification (i.e., O-GlcNAcylation) on proteins is an essential modification in physiology and pathology. Although O-GlcNAcylation is functionally critical, its analysis has never been an easy task. Despite the existence of a number of methods developed in ...
ORGANISM(S): Mus musculus (Mouse) 
2025-10-20 | PXD063995 | Pride
Mouse brain O-glcnac Click chemistry Lc-ms/ms 
ProteomicsDissecting the Molecular Crosstalk between O-GlcNAcylation and Phosphorylation via Quantitative Proteomics and Phosphoproteomics
In this study, we explored the cross-talk between phosphorylation and O-GlcNAcylation using the pancreatic ductal cell line PANC-1 as a model. Proteome and phosphoproteome changes were measured for cells treated with OSMI-1, a specific inhibitor to O-GlcNAc transferase (OGT) and Thiamet G, a specif...
ORGANISM(S): Homo sapiens (Human) 
2026-06-29 | PXD070284 | Pride
Phosphorylation crosstalk o-glcnac 
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